The Structure of the NTPase That Powers DNA Packaging into Sulfolobus Turreted Icosahedral Virus 2

Biochemical reactions powered by ATP hydrolysis are fundamental for the movement of molecules and cellular structures. One such reaction is the encapsidation of the double-stranded DNA (dsDNA) genome of an icosahedrally symmetric virus into a preformed procapsid with the help of a genome-translocating NTPase. Such NTPases have been characterized in detail from both RNA and tailed DNA viruses. We present four crystal structures and the biochemical activity of a thermophilic NTPase, B204, from the nontailed, membrane-containing, hyperthermoacidophilic archaeal dsDNA virus Sulfolobus turreted icosahedral virus 2. These are the first structures of a genome-packaging NTPase from a nontailed, dsDNA virus with an archaeal host. The four structures highlight the catalytic cycle of B204, pinpointing the molecular movement between substrate-bound (open) and empty (closed) active sites. The protein is shown to bind both single-stranded and double-stranded nucleic acids and to have an optimum activity at 80 C and pH 4.5. The overall fold of B204 places it in the FtsK-HerA superfamily of P-loop ATPases, whose cellular and viral members have been suggested to share a DNA-translocating mechanism.

Oksanen, EskoLund University,Lunds universitet,European Spallation Source ESS AB,Stiftelser och övriga anknutna verksamheter,Other Institutions and Utilities(Swepub:lu)esss-eoe (author)
Liljeroos, Lassi (author)
Goldman, Adrian (author)
Kajander, Tommi (author)
Butcher, Sarah J. (author)
European Spallation Source ESS ABStiftelser och övriga anknutna verksamheter (creator_code:org_t)

By the author/editor: Happonen, Lotta; Oksanen, Esko; Liljeroos, Lassi; Goldman, Adrian; Kajander, Tommi; Butcher, Sarah J ...

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